Please use this identifier to cite or link to this item: https://doi.org/10.1007/s002530000347
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dc.titleMolecular studies on isopenicillin N synthases
dc.contributor.authorSim, T.S.
dc.contributor.authorLoke, P.
dc.date.accessioned2016-11-29T01:21:37Z
dc.date.available2016-11-29T01:21:37Z
dc.date.issued2000
dc.identifier.citationSim, T.S., Loke, P. (2000). Molecular studies on isopenicillin N synthases. Applied Microbiology and Biotechnology 54 (1) : 1-8. ScholarBank@NUS Repository. https://doi.org/10.1007/s002530000347
dc.identifier.issn01757598
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/131690
dc.description.abstractThe isopenicillin N synthases isolated thus far are related to oxidases from other microorganisms and plants. These enzymes maintain a non-heme monoferrous-dependent catalytic centre comprising a HisXAsp(53-57)XHis motif and a crucial substrate-binding pocket with an ArgXSer motif for their functionality. The elucidation of these motifs was dependent on information collated from studies on structural chemistry, structural biology, site- directed engineered mutations and biochemical experiments. It is envisaged that these enzymes can potentially be improved through molecular breeding and protein engineering.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1007/s002530000347
dc.sourceScopus
dc.typeOthers
dc.contributor.departmentMICROBIOLOGY
dc.description.doi10.1007/s002530000347
dc.description.sourcetitleApplied Microbiology and Biotechnology
dc.description.volume54
dc.description.issue1
dc.description.page1-8
dc.description.codenAMBID
dc.identifier.isiut000088345800001
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